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Pathway Description
Lysine Degradation
Mus musculus
Category:
Metabolite Pathway
Sub-Category:
Metabolic
Created: 2018-01-21
Last Updated: 2019-08-30
The degradation of L-lysine happens in liver and it is consisted of seven reactions. L-Lysine is imported into liver through low affinity cationic amino acid transporter 2 (cationic amino acid transporter 2/SLC7A2). Afterwards, L-lysine is imported into mitochondria via mitochondrial ornithine transporter 2. L-Lysine can also be obtained from biotin metabolism. L-Lysine and oxoglutaric acid will be combined to form saccharopine by facilitation of mitochondrial alpha-aminoadipic semialdehyde synthase, and then, mitochondrial alpha-aminoadipic semialdehyde synthase will further breaks saccharopine down to allysine and glutamic acid. Allysine will be degraded to form aminoadipic acid through alpha-aminoadipic semialdehyde dehydrogenase. Oxoadipic acid is formed from catalyzation of mitochondrial kynurenine/alpha-aminoadipate aminotransferase on aminoadipic acid. Oxoadipic acid will be further catalyzed to form glutaryl-CoA, and glutaryl-CoA converts to crotonoyl-CoA, and crotonoyl-CoA transformed to 3-hydroxybutyryl-CoA. 3-Hydroxybutyryl-CoA will form Acetyl-CoA as the final product through the intermediate compound: acetoacetyl-CoA. Acetyl-CoA will undergo citric acid cycle metabolism. Carnitine is another key byproduct of lysine metabolism (not shown in this pathway).
References
Lysine Degradation References
Lehninger, A.L. Lehninger principles of biochemistry (4th ed.) (2005). New York: W.H Freeman.
Salway, J.G. Metabolism at a glance (3rd ed.) (2004). Alden, Mass.: Blackwell Pub.
Papes F, Kemper EL, Cord-Neto G, Langone F, Arruda P: Lysine degradation through the saccharopine pathway in mammals: involvement of both bifunctional and monofunctional lysine-degrading enzymes in mouse. Biochem J. 1999 Dec 1;344 Pt 2:555-63.
Pubmed: 10567240
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Pubmed: 15489334
Huttlin EL, Jedrychowski MP, Elias JE, Goswami T, Rad R, Beausoleil SA, Villen J, Haas W, Sowa ME, Gygi SP: A tissue-specific atlas of mouse protein phosphorylation and expression. Cell. 2010 Dec 23;143(7):1174-89. doi: 10.1016/j.cell.2010.12.001.
Pubmed: 21183079
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Pubmed: 16141072
Yu P, Mosbrook DM, Tagle DA: Genomic organization and expression analysis of mouse kynurenine aminotransferase II, a possible factor in the pathophysiology of Huntington's disease. Mamm Genome. 1999 Sep;10(9):845-52.
Pubmed: 10441733
Nomura M, Takihara Y, Shimada K: Isolation of a cDNA clone encoding mouse 3-hydroxyacyl CoA dehydrogenase. Gene. 1995 Jul 28;160(2):309-10. doi: 10.1016/0378-1119(95)00205-k.
Pubmed: 7642117
Herbst R, Barton JL, Nicklin MJ: A mammalian homolog of the bacterial monomeric sarcosine oxidases maps to mouse chromosome 11, close to Cryba1. Genomics. 1997 Dec 15;46(3):480-2. doi: 10.1006/geno.1997.5050.
Pubmed: 9441754
Koeller DM, DiGiulio KA, Angeloni SV, Dowler LL, Frerman FE, White RA, Goodman SI: Cloning, structure, and chromosome localization of the mouse glutaryl-CoA dehydrogenase gene. Genomics. 1995 Aug 10;28(3):508-12. doi: 10.1006/geno.1995.1182.
Pubmed: 7490088
This pathway was propagated using PathWhiz -
Pon, A. et al. Pathways with PathWhiz (2015) Nucleic Acids Res. 43(Web Server issue): W552–W559.
Propagated from SMP0000037
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